Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2,4-dienoyl-CoA reductase, mitochondrial

Gene

Decr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA (By similarity).By similarity

Catalytic activityi

Trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911NADPBy similarity
Binding sitei91 – 911SubstrateBy similarity
Binding sitei117 – 1171NADPBy similarity
Binding sitei119 – 1191SubstrateBy similarity
Binding sitei149 – 1491SubstrateBy similarity
Active sitei199 – 1991Proton acceptorSequence analysis
Binding sitei214 – 2141NADPBy similarity
Binding sitei251 – 2511SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 716NADPBy similarity
Nucleotide bindingi240 – 2434NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiR-MMU-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.

Names & Taxonomyi

Protein namesi
Recommended name:
2,4-dienoyl-CoA reductase, mitochondrial (EC:1.3.1.34)
Alternative name(s):
2,4-dienoyl-CoA reductase [NADPH]
Short name:
4-enoyl-CoA reductase [NADPH]
Gene namesi
Name:Decr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1914710. Decr1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434MitochondrionBy similarityAdd
BLAST
Chaini35 – 3353012,4-dienoyl-CoA reductase, mitochondrialPRO_0000031966Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-acetyllysine; alternateCombined sources
Modified residuei42 – 421N6-succinyllysine; alternateCombined sources
Modified residuei49 – 491N6-acetyllysine; alternateCombined sources
Modified residuei49 – 491N6-succinyllysine; alternateCombined sources
Modified residuei69 – 691PhosphothreonineBy similarity
Modified residuei73 – 731N6-succinyllysineCombined sources
Modified residuei97 – 971N6-acetyllysine; alternateCombined sources
Modified residuei97 – 971N6-succinyllysine; alternateCombined sources
Modified residuei106 – 1061N6-acetyllysine; alternateCombined sources
Modified residuei106 – 1061N6-succinyllysine; alternateCombined sources
Modified residuei244 – 2441N6-acetyllysine; alternateCombined sources
Modified residuei244 – 2441N6-succinyllysine; alternateCombined sources
Modified residuei260 – 2601N6-acetyllysine; alternateCombined sources
Modified residuei260 – 2601N6-succinyllysine; alternateCombined sources
Modified residuei315 – 3151N6-acetyllysineCombined sources
Modified residuei319 – 3191N6-acetyllysine; alternateCombined sources
Modified residuei319 – 3191N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CQ62.
MaxQBiQ9CQ62.
PaxDbiQ9CQ62.
PRIDEiQ9CQ62.

PTM databases

iPTMnetiQ9CQ62.
PhosphoSiteiQ9CQ62.

Expressioni

Gene expression databases

BgeeiQ9CQ62.
CleanExiMM_DECR1.
ExpressionAtlasiQ9CQ62. baseline and differential.
GenevisibleiQ9CQ62. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ9CQ62. 4 interactions.
MINTiMINT-1860375.
STRINGi10090.ENSMUSP00000029877.

Structurei

3D structure databases

ProteinModelPortaliQ9CQ62.
SMRiQ9CQ62. Positions 37-328.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0725. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG005465.
InParanoidiQ9CQ62.
KOiK13236.
OMAiFQSKFFP.
OrthoDBiEOG7KH9K9.
PhylomeDBiQ9CQ62.
TreeFamiTF315256.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQ62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLGRAFFA GVSRLPCDPG PQRFFSFGTK TLYQSKDAPQ SKFFQPVLKP
60 70 80 90 100
MLPPDAFQGK VAFITGGGTG LGKAMTTFLS TLGAQCVIAS RNIDVLKATA
110 120 130 140 150
EEISSKTGNK VHAIRCDVRD PDMVHNTVLE LIKVAGHPDV VINNAAGNFI
160 170 180 190 200
SPSERLTPNG WKTITDIVLN GTAYVTLEIG KQLIKAQKGA AFLAITTIYA
210 220 230 240 250
ESGSGFVMPS SSAKSGVEAM NKSLAAEWGR YGMRFNIIQP GPIKTKGAFS
260 270 280 290 300
RLDPTGRFEK EMIDRIPCGR LGTMEELANL ATFLCSDYAS WINGAVIRFD
310 320 330
GGEEVFLSGE FNSLKKVTKE EWDIIEGLIR KTKGS
Length:335
Mass (Da):36,214
Last modified:June 1, 2001 - v1
Checksum:iC064AC03F818E25A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031G → V in BAB22333 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002756 mRNA. Translation: BAB22333.1.
AK004725 mRNA. Translation: BAB23508.1.
AK015692 mRNA. Translation: BAB29933.1.
BC046972 mRNA. Translation: AAH46972.1.
CCDSiCCDS17985.1.
RefSeqiNP_080448.1. NM_026172.3.
UniGeneiMm.393293.

Genome annotation databases

EnsembliENSMUST00000029877; ENSMUSP00000029877; ENSMUSG00000028223.
GeneIDi67460.
KEGGimmu:67460.
UCSCiuc008sbm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002756 mRNA. Translation: BAB22333.1.
AK004725 mRNA. Translation: BAB23508.1.
AK015692 mRNA. Translation: BAB29933.1.
BC046972 mRNA. Translation: AAH46972.1.
CCDSiCCDS17985.1.
RefSeqiNP_080448.1. NM_026172.3.
UniGeneiMm.393293.

3D structure databases

ProteinModelPortaliQ9CQ62.
SMRiQ9CQ62. Positions 37-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CQ62. 4 interactions.
MINTiMINT-1860375.
STRINGi10090.ENSMUSP00000029877.

PTM databases

iPTMnetiQ9CQ62.
PhosphoSiteiQ9CQ62.

Proteomic databases

EPDiQ9CQ62.
MaxQBiQ9CQ62.
PaxDbiQ9CQ62.
PRIDEiQ9CQ62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029877; ENSMUSP00000029877; ENSMUSG00000028223.
GeneIDi67460.
KEGGimmu:67460.
UCSCiuc008sbm.1. mouse.

Organism-specific databases

CTDi1666.
MGIiMGI:1914710. Decr1.

Phylogenomic databases

eggNOGiKOG0725. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG005465.
InParanoidiQ9CQ62.
KOiK13236.
OMAiFQSKFFP.
OrthoDBiEOG7KH9K9.
PhylomeDBiQ9CQ62.
TreeFamiTF315256.

Enzyme and pathway databases

ReactomeiR-MMU-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.

Miscellaneous databases

NextBioi324642.
PROiQ9CQ62.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ62.
CleanExiMM_DECR1.
ExpressionAtlasiQ9CQ62. baseline and differential.
GenevisibleiQ9CQ62. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung and Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-49; LYS-73; LYS-97; LYS-106; LYS-244; LYS-260 AND LYS-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-49; LYS-97; LYS-106; LYS-244; LYS-260; LYS-315 AND LYS-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDECR_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ62
Secondary accession number(s): Q9DCI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.